PMID:17046713

Citation	Mellroth, P and Steiner, H (2006) PGRP-SB1: an N-acetylmuramoyl L-alanine amidase with antibacterial activity. Biochem. Biophys. Res. Commun. 350:994-9
Abstract	The peptidoglycan recognition protein (PGRP) family is conserved from insects to mammals and is involved in immune regulation and bacterial clearance. They form at least three functional classes; receptors required for immune gene expression; amidases that degrade peptidoglycan and scavenge the tissues from immune-stimulating peptidoglycan; and as proteins with antibacterial activity. We here report that PGRP-SB1 is an N-acetylmuramoyl l-alanine amidase, which (in contrast to the previously described PGRP-amidases) shows antibacterial activity. PGRP-SB1 is highly active against peptidoglycans that have a diaminopimelic acid (DAP) residue in the cross-linking peptide, but lack activity to most lysine-containing peptidoglycans. The antibacterial activity is pronounced against Bacillus megaterium with an LD(50) of 1.5microg ml(-1). The bactericidal effect of PGRP-SB1 is dependent on its enzymatic activity, as the zinc co-factor is essential. The bactericidal mode of action is thus different from non-enzymatic vertebrate PGRPs that have been reported to be antibacterial.
Links	PubMed Online version:10.1016/j.bbrc.2006.09.139
Keywords	Anti-Bacterial Agents/administration & dosage; Bacillus megaterium/cytology; Bacillus megaterium/drug effects; Carrier Proteins/administration & dosage; Cell Survival/drug effects; Dose-Response Relationship, Drug; Drosophila Proteins/administration & dosage
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
DROME:PGSB1		GO:0008745: N-acetylmuramoyl-L-alanine amidase activity	ECO:0000314:		F		Fig. 2. PGRP-SB1 possesses N-acetylmuramoyl l-alanine amidase activity.	complete CACAO 12145

References

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